Polymorphic cross-seeding amyloid assemblies of amyloid-β and human islet amyloid polypeptide

2015 ◽  
Vol 17 (35) ◽  
pp. 23245-23256 ◽  
Author(s):  
Mingzhen Zhang ◽  
Rundong Hu ◽  
Hong Chen ◽  
Yung Chang ◽  
Jie Ma ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Type 2 Diabetes ◽  
Alzheimer's Disease ◽  
Islet Amyloid Polypeptide ◽  
Amyloid Β ◽  
Epidemiological Studies ◽  
Human Islet ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide

Epidemiological studies have shown that the development of Alzheimer's disease (AD) is associated with type 2 diabetes (T2D), but it still remains unclear how AD and T2D are connected.

scholarly journals Hsp72 (HSPA1A) Prevents Human Islet Amyloid Polypeptide Aggregation and Toxicity: A New Approach for Type 2 Diabetes Treatment

PLoS ONE ◽  
2016 ◽  
Vol 11 (3) ◽  
pp. e0149409 ◽  
Author(s):  
Paola C. Rosas ◽  
Ganachari M. Nagaraja ◽  
Punit Kaur ◽  
Alexander Panossian ◽  
Georg Wickman ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Islet Amyloid Polypeptide ◽  
Human Islet ◽  
Diabetes Treatment ◽  
Islet Amyloid ◽  
New Approach ◽  
Human Islet Amyloid Polypeptide ◽  
Type 2 Diabetes Treatment

scholarly journals Stabilization and structural analysis of a membrane-associated hIAPP aggregation intermediate

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Diana C Rodriguez Camargo ◽  
Kyle J Korshavn ◽  
Alexander Jussupow ◽  
Kolio Raltchev ◽  
David Goricanec ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Cell Death ◽  
Islet Amyloid Polypeptide ◽  
Amyloid Β ◽  
Md Simulations ◽  
Human Islet ◽  
Amyloid Formation ◽  
Islet Amyloid ◽  
Induce Cell Death

Membrane-assisted amyloid formation is implicated in human diseases, and many of the aggregating species accelerate amyloid formation and induce cell death. While structures of membrane-associated intermediates would provide tremendous insights into the pathology and aid in the design of compounds to potentially treat the diseases, it has not been feasible to overcome the challenges posed by the cell membrane. Here, we use NMR experimental constraints to solve the structure of a type-2 diabetes related human islet amyloid polypeptide intermediate stabilized in nanodiscs. ROSETTA and MD simulations resulted in a unique β-strand structure distinct from the conventional amyloid β-hairpin and revealed that the nucleating NFGAIL region remains flexible and accessible within this isolated intermediate, suggesting a mechanism by which membrane-associated aggregation may be propagated. The ability of nanodiscs to trap amyloid intermediates as demonstrated could become one of the most powerful approaches to dissect the complicated misfolding pathways of protein aggregation.

BACE2 suppression promotes β-cell survival and function in a model of type 2 diabetes induced by human islet amyloid polypeptide overexpression

2017 ◽  
Vol 74 (15) ◽  
pp. 2827-2838 ◽  
Author(s):  
Gema Alcarraz-Vizán ◽  
Carlos Castaño ◽  
Montse Visa ◽  
Joel Montane ◽  
Joan-Marc Servitja ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Cell Survival ◽  
Islet Amyloid Polypeptide ◽  
Human Islet ◽  
Β Cell ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide ◽  
And Function

scholarly journals Copper Coordination Features of Human Islet Amyloid Polypeptide: The Type 2 Diabetes Peptide

2016 ◽  
Vol 55 (20) ◽  
pp. 10727-10740 ◽  
Author(s):  
Carolina Sánchez-López ◽  
Rodrigo Cortés-Mejía ◽  
Marco C. Miotto ◽  
Andres Binolfi ◽  
Claudio O. Fernández ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Islet Amyloid Polypeptide ◽  
Human Islet ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide ◽  
Copper Coordination
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